ID A0A3Q1FWF6_9TELE Unreviewed; 1136 AA.
AC A0A3Q1FWF6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
GN Name=HDAC5 {ECO:0000313|Ensembl:ENSAPOP00000010750.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000010750.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000010750.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. {ECO:0000256|PIRNR:PIRNR037911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000256|PIRNR:PIRNR037911};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037911}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738,
CC ECO:0000256|PIRNR:PIRNR037911}.
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DR AlphaFoldDB; A0A3Q1FWF6; -.
DR STRING; 80966.ENSAPOP00000010750; -.
DR Ensembl; ENSAPOT00000018165.1; ENSAPOP00000010750.1; ENSAPOG00000013271.1.
DR GeneTree; ENSGT00940000160534; -.
DR InParanoid; A0A3Q1FWF6; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0072114; P:pronephros morphogenesis; IEA:Ensembl.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd10164; ClassIIa_HDAC5_Gln-rich-N; 1.
DR Gene3D; 6.10.250.1550; -; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR046949; HDAC4/5/7/9.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF11; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 113..201
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 714..1032
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 60..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 156..214
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 246..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 843
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 706
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 714
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 791
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 1016
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1136 AA; 122771 MW; C07F0660AE93CF74 CRC64;
MLLHPTVSGL CAMLQTIYET ESCFSSASTD SHHQPLELLS DSRGSGAAMP TALVEVKSSL
PSGMQSPVGT ASEQRGGGGE GGGGPAEGPG GGGSPMDLRT EPRVGALSGG AAVDTALREQ
QLQQELVLLK QQQELQKQLL FAEFQKKHEV LTRQHEVQLQ EHLKQQQELL AAKRQQELEQ
KRKLEQQRHE EQEKQRLEQQ LLLLRNKEKG KESAIASTEV KLKLQEFLLS KKEPGPGGLN
HSFSPKCWGA QHTSLEQSSP PQSNTPGTPP SYKLPPLLGN YEGKDDFPLR KTVSEPNLKV
RSRLKQKVAE RRSSPLLRRK DGTVISTFKK RAIEISVSSL CNSAPGSGPS SPNSSNTAIA
NGNTGSVPNI QTELRSLHQT LGADGTLSPL SLYTSPSLPN ISLGLPANTH ITTSQKLSTQ
QEAELQAIQS LRGGGALTGK FLSTSSLPAG VGHDVETPPP SSHSAHSSLL QHVLLLEQAR
QQTAMLVPMY SQSPLVTAER GVSSGMRSVS KLPRHRPLAR TQSAPLPQSP QALQQLVVQQ
QHQHFLEKHY KMLSKGAELP RPPPTHPEET EEELTETNDM QEDDVGAGLH RLQKEGSDDS
TPSSERLGVL VKGEEERGSI HVKGESTESE LDEEEEDDEV IQLREGDEEE RGSYTQALQQ
LGVFQSSLPH RPLGRAQSSP AATVNPIKHL FTTGLVYDSL MLKHQCVCGN AHIHPEHAGR
VQSIWSRLQE TGLLGRCERI RGRKASLDEI QSVHSEFHTL LYGTSPLNRH KLDHKKLLGP
ISQKMYAVLP CGGIGVDSDT VWNEMHSSAA VRMAVGSVIE LAFRVAAGEL KNGFAVVRPP
GHHAEESTAM GFCFFNSVAI TAKLLQQKLG VGKILIVDWD IHHGNGTQQA FYSDPNVLYI
SLHRYDDGNF FPGSGAPEEV GSGAGVGFNV NIAWTGGVEP PMGDVEYLTA FRSVVMPIAQ
QFSPDVVLVS AGFDAVEGHQ SPLGGYNVSA KCFGQLSQLL MGLAGGRVVM ALEGGHDLTA
ICDASEACVA ALLGDPCDSM FQWPQEQPCP KACASLERVI EIQSKHWSCL QSLSQTSGHS
LLDGPLAAQG QSEKDEAETV SAMASLSVDV EQPGSVPDNT ETSRSTEEPM EEEPVL
//
